Evidence map›Paper›PMID 23527380›Full record

ArticleChemical communications (Cambridge, England)2013

Molecular insights into the reversible formation of tau protein fibrils.

Yin Luo, Paul Dinkel, Xiang Yu, Martin Margittai, Jie Zheng, Ruth Nussinov, Guanghong Wei, Buyong Ma

Abstract read
In one paragraph

Article in Chemical communications (Cambridge, England), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.8field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. The distinct structural preferences of tau protein repeat domains.Chemical communications (Cambridge, England) · 2018
    Article
  8. Amyloidogenesis of Tau protein.Protein science : a publication of the Protein Society · 2017
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 5 institutions in 3 countries.

Yin LuoState Key Laboratory of Surface Physics, Department of Physics, Fudan University, Shanghai, PR China.
Paul Dinkel
Xiang Yu
Martin Margittai
Jie Zheng
Ruth Nussinov
Guanghong Wei
Buyong Ma
Science Applications International Corporation (United States) · USUniversity of Akron · USUniversity of Denver · USFudan University · CNState Key Laboratory of Surface Physics

Funding

Protein Structure, Stability, and Amyloid FormationZIABC010440 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$11.8M
Method Development: Efficient Computer Vision Based AlgorithmsZIABC010442 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$2.4M
LINKING TAU FILAMENT STRUCTURE TO PHENOTYPIC DIVERSITY IN HUMAN TAUOPATHIESR01NS076619 · NINDS · UNIVERSITY OF DENVER (COLORADO SEMINARY) · PI MARGITTAI, MARTIN · 2011 to 2014
$1.2M
CCR NIH HHS HHSN261200800001CNCI NIH HHS HHSN261200800001ENINDS NIH HHS R01 NS076619NINDS NIH HHS R01NS076619
6 · The paper itself

Abstract

We computationally and experimentally showed that tau protein fibrils can be formed at high temperature. When cooled, the fibrils dissociate back to monomers. Heparin promotes tau fibril formation and prevents its reversion. Our results revealed the physicochemical mechanism of reversible formation of tau fibrils.

Indexed as

AmyloidHeparinHot Temperaturetau ProteinsAmyloidHeparintau Proteins

Identifiers

PMID23527380
PMCPMC3637047
OpenAlexW1979891321

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.